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1980•Infection and ImmunityOpen access

Binding of cholesterol by sulfhydryl-activated cytolysins

Mary K. Johnson, C Geoffroy, Joseph E. Alouf

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Abstract

The binding of cholesterol by pneumolysin, alveolysin, and streptolysin O has been demonstrated. The properties of the cytolysin-cholesterol interaction parallel those of cytolysin-erythrocyte interaction in that the reaction is rapid, temperature independent, decreased at elevated pH, and shows the same specificity with respect to other related sterols. However, oxidized or p-hydroxymercuribenzoate-treated thoxin showed no decrease in cholesterol-binding activity, whereas the ability of cytolysin to bind to erythrocytes was modified by such treatment.

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The binding of cholesterol by pneumolysin, alveolysin, and streptolysin O has been demonstrated. The properties of the cytolysin-cholesterol interaction parallel those of cytolysin-erythrocyte interaction in that the reaction is rapid, temperature independent, decreased at elevated pH, and shows the same specificity with respect to other related sterols. However, oxidized or p-hydroxymercuribenzoate-treated thoxin showed no decrease in cholesterol-binding activity, whereas the ability of cytolysin to bind to erythrocytes was modified by such treatment.

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Available abstract

The binding of cholesterol by pneumolysin, alveolysin, and streptolysin O has been demonstrated. The properties of the cytolysin-cholesterol interaction parallel those of cytolysin-erythrocyte interaction in that the reaction is rapid, temperature independent, decreased at elevated pH, and shows the same specificity with respect to other related sterols. However, oxidized or p-hydroxymercuribenzoate-treated thoxin showed no decrease in cholesterol-binding activity, whereas the ability of cytolysin to bind to erythrocytes was modified by such treatment.

Key concepts: Cytolysin, Streptolysin, Biology, Cholesterol, Biochemistry, Pneumolysin, Lysis, Microbiology

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